Detailed Modes of Action and Biochemical Characterization of endo-Arabinanase from Bacillus licheniformis DSM13

Jung-Mi Park; Myoung-Uoon Jang; Jung-Hyun Kang; Min-Jeong Kim; So-Won Lee; Yeong Bok Song; Chul-Soo Shin; Nam Soo Han; Tae-Jip Kim

doi:10.1007/s12275-012-2489-3

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Detailed Modes of Action and Biochemical Characterization of endo-Arabinanase from Bacillus licheniformis DSM13: Jung-Mi Park ¹, Myoung-Uoon Jang ¹, Jung-Hyun Kang ¹, Min-Jeong Kim ¹, So-Won Lee ¹, Yeong Bok Song ², Chul-Soo Shin ³, Nam Soo Han ¹, Tae-Jip Kim ¹; Journal of Microbiology 2012;50(6):1041-1046.
DOI: https://doi.org/10.1007/s12275-012-2489-3
Published online: December 30, 2012

¹Department of Food Science and Technology, Chungbuk National University, Cheongju 361-763, Republic of Korea, ²Sejeon Food Research Institute, Sejeon Co., Seongnam 462-807, Republic of Korea, ³Advanced Protein Technology Co., Suwon 443-813, Republic of Korea¹Department of Food Science and Technology, Chungbuk National University, Cheongju 361-763, Republic of Korea, ²Sejeon Food Research Institute, Sejeon Co., Seongnam 462-807, Republic of Korea, ³Advanced Protein Technology Co., Suwon 443-813, Republic of Korea

Corresponding author: Tae-Jip Kim , Tel: +82-43-261-3354,

Received: 6 September 2012 • Accepted: 19 September 2012

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Abstract

An endo-arabinanase (BLABNase) gene from Bacillus licheniformis DSM13 was cloned and expressed in Escherichia coli, and the biochemical properties of its encoded enzyme were characterized. The BLABNase gene consists of a single open reading frame of 987 nucleotides that encodes 328 amino acids with a predicted molecular mass of about 36 kDa. BLABNase exhibited the highest activity against debranched α-(1,5)-arabinan in 50 mM sodium acetate buffer (pH 6.0) at 55°C. Enzymatic characterization revealed that BLABNase hydrolyzes debranched or linear arabinans with a much higher activity than branched arabinan from sugar beet. Enzymatic hydrolysis pattern analyses demonstrated BLABNase to be a typical endo-(1,5)-α-L-arabinanase (EC 3.2.1.99) that randomly cleaves the internal α-(1,5)-linked L-arabinofuranosyl residues of a branchless arabinan backbone to release arabinotriose mainly, although a small amount of arabino-oligosaccharide intermediates is also liberated. Our results indicated that BLABNase acts preferentially along with the oligosaccharides longer than arabinopentaose, thus enabling the enzymatic production of various arabinooligosaccharides.

Keywords: Bacillus licheniformis DSM13;endo-(1;5)-α-L-arabinanase;gene expression;enzymatic hydrolysis patterns;arabino-oligosaccharides production

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Detailed Modes of Action and Biochemical Characterization of endo-Arabinanase from Bacillus licheniformis DSM13

J. Microbiol. 2012;50(6):1041-1046. Published online December 30, 2012

DOI: https://doi.org/10.1007/s12275-012-2489-3

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